Proteome mapping of mature pollen ofArabidopsis thaliana

Holmes‐Davis, Rachel; Tanaka, Charlene K.; Vensel, William H.; Hurkman, William J.; McCormick, Sheila

doi:10.1002/pmic.200402011

Cited by 221 publications

(232 citation statements)

References 65 publications

(53 reference statements)

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“…A similar pattern of expression of these PMEs was obtained previously in two transcriptomic analyses of dry pollen grains and pollen tubes (Wang et al, 2008;Qin et al, 2009). Moreover, proteomic analyses of Arabidopsis revealed the presence of at least three PMEs in mature pollen grains: PME37, PPME1, and PME48 (Holmes- Davis et al, 2005;Ge et al, 2011). Similarly, at least two PMEs were found in the Figure 6.…”

Section: Discussionsupporting

confidence: 83%

PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

et al. 2014

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Germination of pollen grains is a crucial step in plant reproduction. However, the molecular mechanisms involved remain unclear. We investigated the role of PECTIN METHYLESTERASE48 (PME48), an enzyme implicated in the remodeling of pectins in Arabidopsis (Arabidopsis thaliana) pollen. A combination of functional genomics, gene expression, in vivo and in vitro pollen germination, immunolabeling, and biochemical analyses was used on wild-type and Atpme48 mutant plants. We showed that AtPME48 is specifically expressed in the male gametophyte and is the second most expressed PME in dry and imbibed pollen grains. Pollen grains from homozygous mutant lines displayed a significant delay in imbibition and germination in vitro and in vivo. Moreover, numerous pollen grains showed two tips emerging instead of one in the wild type. Immunolabeling and Fourier transform infrared analyses showed that the degree of methylesterification of the homogalacturonan was higher in pme482/2 pollen grains. In contrast, the PME activity was lower in pme482/2, partly due to a reduction of PME48 activity revealed by zymogram. Interestingly, the wild-type phenotype was restored in pme482/2 with the optimum germination medium supplemented with 2.5 mM calcium chloride, suggesting that in the wild-type pollen, the weakly methylesterified homogalacturonan is a source of Ca 2+ necessary for pollen germination. Although pollen-specific PMEs are traditionally associated with pollen tube elongation, this study provides strong evidence that PME48 impacts the mechanical properties of the intine wall during maturation of the pollen grain, which, in turn, influences pollen grain germination.

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Section: Discussionsupporting

confidence: 83%

PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

et al. 2014

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“…The mature male germ cell proteome has been studied in model species such as plants [22] or worms [23]. In man, specific approaches to target subcellular organelles or compartments have been successfully used [11,[24][25][26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

228

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Conventional 1-DE has in the past provided a wealth of information concerning the major sperm proteins. However, so far there are relatively few reports exploiting the potential of the present proteomic tools to identify and to study additional yet-unidentified important proteins present in human spermatozoa. In the present work, 2-DE of proteins extracted from human normozoospermic spermatozoa led to the resolution of over 1000 spots. Subsequent excision from the gels of 145 spots and MALDI-TOF MS analysis allowed the identification of 98 different proteins. The function of these proteins turned out to be energy production (23%), transcription, protein synthesis, transport, folding and turnover (23%), cell cycle, apoptosis and oxidative stress (10%), signal transduction (8%), cytoskeleton, flagella and cell movement (10%), cell recognition (7%), metabolism (6%) and unknown function (11%). As many as 23% of the proteins identified have not been previously described as being expressed in human spermatozoa. The present data provide an important clue towards determining the function of these proteins and opens up the possibility to perform additional experiments.

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“…Recent proteomics studies from Arabidopsis (12,13) and rice (14) have revealed that mature pollen presynthesizes a complement of proteins required for pollen function, including those implicated in protein synthesis and carbohydrate/energy metabolism. Dai et al (14) showed that these functional categories related to carbohydrate/energy metabolism, wall metabolism, protein synthesis and degradation, and signaling are overrepresented in the proteome.…”

mentioning

confidence: 99%

Proteomics Identification of Differentially Expressed Proteins Associated with Pollen Germination and Tube Growth Reveals Characteristics of Germinated Oryza sativa Pollen

Dai

Chen

Chong

et al. 2007

Molecular & Cellular Proteomics

136

134

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Mature pollen from most plant species is metabolically quiescent; however, after pollination, it germinates quickly and gives rise to a pollen tube to transport sperms into the embryo sac. Because methods for collecting a large amount of in vitro germinated pollen grains for transcriptomics and proteomics studies from model plants of Arabidopsis and rice are not available, molecular information about the germination developmental process is lacking. Here we describe a method for obtaining a large quantity of in vitro germinating rice pollen for proteomics study. Two-dimensional electrophoresis of ϳ2300 protein spots revealed 186 that were differentially expressed in mature and germinated pollen. Most showed a changed level of expression, and only 66 appeared to be specific to developmental stages. Furthermore 160 differentially expressed protein spots were identified on mass spectrometry to match 120 diverse protein species. These proteins involve different cellular and metabolic processes with obvious functional skew toward wall metabolism, protein synthesis and degradation, cytoskeleton dynamics, and carbohydrate/energy metabolism. Wall metabolism-related proteins are prominently featured in the differentially expressed proteins and the pollen proteome as compared with rice sporophytic proteomes. Our study also revealed multiple isoforms and differential expression patterns between isoforms of a protein. These results provide novel insights into pollen function specialization. Pollen of flowering plants, generated in diploid sporophytic plants via meiosis followed by two cycles of mitosis, contains three haploid genomes and is a highly reduced organism. Mature pollen grains from most plant species are metabolically quiescent. However, during pollination, they can quickly germinate and give rise to a polarly growing pollen tube whereby the pollen interacts with pistils and then delivers two sperms into the embryo sac to initiate double fertilization. Besides having biological importance, pollen germination and tube growth have been considered unique developmental processes for studying cell polar establishment, cell differentiation, cell fate determination, and cell-to-cell recognition. Thus, the molecular mechanisms underlining the specific cellular programs have been the focus of investigation over the past 50 years (1). However, until now, only a limited number of genes encoding coat/wall proteins or signal molecules have been shown to be essential for pollen germination, tube growth, and interaction of the tube and stigma (1-7).Recent analyses of mature pollen of Arabidopsis revealed the transcriptome to have reduced complexity and a higher proportion of selectively expressed transcripts than sporophytic tissues (8 -10). As well, about one-third of the genes expressed in vegetative tissues are not expressed in the pollen (8). The observation suggests that the transcriptional characteristics involve pollen function specialization. Furthermore these studies determined that pollen transcriptome has a functiona...

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Proteome mapping of mature pollen ofArabidopsis thaliana

Cited by 221 publications

References 65 publications

PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

PECTIN METHYLESTERASE48 Is Involved in Arabidopsis Pollen Grain Germination

Proteomic identification of human sperm proteins

Proteomics Identification of Differentially Expressed Proteins Associated with Pollen Germination and Tube Growth Reveals Characteristics of Germinated Oryza sativa Pollen

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